IONTOSORB - Bead Cellulose Derivatives
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Iontosorb CM

is a weakly acidic cation exchanger based on Bead Cellulose with carboxylic functional groups:

Chemical Structure (1230 bytes)

The total volume capacity can be in the range 0.05 - 0.25 mmol/ml, the adequate mass capacity is 0.8 to 1.2 mmol/g dry matter. According to the customerīs demands the sorbent volume capacity can be varied in the range given by the mass capacity and water content. The water content of Iontosorb CM moves in the connection with the volume capacity in the range 74 to 89 %.

Iontosorb CM is suitable for chromatographic separations of basic proteins, basic amino acids, peptides, lipids and similar substances. Beside that, it may be used for enzyme immobilization.

Applications of Iontosorb CM

Iontosorb CM can be used in the following applications:

 

ISOLATION AND CHARACTERISATION OF THE PROTEOLITIC ENZYMES OF CARP HEPATOPANCREAS

M. Kminkova, Z. Moucka, Jiri Kucera

Potrav. vedy, 15 (1997) 351-362

Trypsin and Chymotripsyn activity in pooled fractions obtained from iontosorb CM column (pH 6.0)

Column 2 x 8 cm equilibrated with 10 mM Tris-HCl pH 6.0 buffer, containing 10 mM calcium chloride

Adsorbed fractions were elued with 1 M NaCl in starting buffer after washing-out the unadsorbed proteins.

Original articles as full texts are available in the information CD of the firm Iontosorb.

 

USE OF BEAD CELLULOSE DERIVATIVES TO ISOLATION OF BACTERIAL ALKALINE PROTEINASE BY COLUMN LIQUID CHROMATOGRAPHY

P. Gemeiner, V. Spanik, A. Snajdrova, E. Stratilova, M. Horvathova, D. Hagarova and O. Markovic

Folia Microbiol. 36 (1991) 283-293

Semi-preparative ion exchange chromatography of alkaline proteinase on Iontosorb CM

The column 21 x 130 mm was equilibrated with phosphate buffer and eluted with linear gradients of 0-0.5 and 0.5-1 mol/L NaCl, respectively, in the above buffer; combined fractions (7-10) from theproceding IEC dialyzed against phosphate buffer were loaded; the flow rate 0.5 mL/min, 5 mL fractions were colected 

N - fraction number, P - proteins (mg, circles), A620/h - proteolytic activity (squares), NaCl gradient (mol/L, dashed line).

Original articles as full texts are available in the information CD of the firm Iontosorb.

 

MAGNETIC CATION EXCHANGE ISOLATION OF LYSOZYME FROM NATIVE HEG EGG WHITE

I. Safarik, Z. Sabatkova, O. Tokar, M. Safarikova

Food Technol. Biotechnol., 45 (2007) 355-359

Fast protein liquid chromatography of original egg white (top), eluate from Iontosorb MG CM 100 (middle) and eluate from Iontosorb MG SHP 100 (bottom)

 

Electrophoretic patterns of egg white proteins and lysozyme isolated by Iontosorb MG CM 100

Lane 1- molecular mass markers; lane 2-egg white (9.3 ug of proteins loaded); lane 3-egg white after finishing the adsorption process (8.1 ug of proteins loaded); lane 4-lysozyme after elution from Iontosorb MG CM 100 (8.75 ug of proteins loaded); lane 5-commercial lysozyme (Fluka, Germanny, 12 ug of proteins loaded). Arrow indicates the lysozyme position.

 

Equilibrium adsorption isotherms of hen egg white lysozyme using Iontosorb MG CM 100 (full triangles) and Iontosorb MG SHP 100 (full squares) as adsorbents

Ceq - equilibrium liquid-phase concentration of the unadsorbed (free) lysozyme; qeq - equilibrium solid-phase concentration of the adsorbed lysozyme

Original articles as full texts are available in the information CD of the firm Iontosorb or Isolation of  LYSOZYME .

 

 

Technical Parameters

Porozity Type Particle Size
[ um ]
CM  100 30 - 50
50 - 80
80 - 100
100 - 250
250 - 500
CM  200 50 - 80
80 - 100
100 - 250
250 - 500
CM  500 50 - 80
80 - 100
100 - 250
250 - 500